Conserved Protein Domain Family
SH3_SH3RF2_2

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cd11932: SH3_SH3RF2_2 
Second Src Homology 3 domain of SH3 domain containing ring finger 2
SH3RF2 is also called POSHER (POSH-eliminating RING protein) or HEPP1 (heart protein phosphatase 1-binding protein). It acts as an anti-apoptotic regulator of the JNK pathway by binding to and promoting the degradation of SH3RF1 (or POSH), a scaffold protein that is required for pro-apoptotic JNK activation. It may also play a role in cardiac functions together with protein phosphatase 1. SH3RF2 contains an N-terminal RING finger domain and three SH3 domains. This model represents the second SH3 domain, located C-terminal of the first SH3 domain at the N-terminal half, of SH3RF2. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Statistics
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PSSM-Id: 212865
Aligned: 3 rows
Threshold Bit Score: 116.478
Created: 7-Dec-2011
Updated: 2-Oct-2020
Structure
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Aligned Rows:
 
peptide ligand
Feature 1:peptide ligand binding site [polypeptide binding site]
Evidence:
  • Comment:based on the binding of peptide ligands to the SH3 domains of other superfamily members
  • Comment:SH3 domains typically bind proline-rich ligands, preferentially to PxxP motifs.
  • Citation:PMID 7664083
  • Citation:PMID 7735837
  • Comment:flanking hinge and loops (RT and n-Src) confer sequence specificity for ligand residues outside the core binding motif

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:

Feature 1             # #  #        #                 ##            # ## 
Q8TEC5       191 LCRALYNFDLRGK.[6].DCLTFLKDDIITVISRVDENWAEGKLGDKVGIFPILFV 247 human
NP_001085119 188 LCKAIYKFDLKEK.[5].DCLKFQKDDVISVIRRMDENWAEGKLGDQVGIFPLMFV 243 African clawed frog
XP_003224154 192 LCRALYNFDLKSR.[6].ECLPFHKGDIITVISRVDENWAEGKIGDRTGIFPILFV 248 green anole

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